title: Influence of high pressure on the dimerization of ToxR, a protein involved in bacterial signal transduction.
abstract: High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.
authors.affiliation: Lehrstuhl für Technische Mikrobiologie, Technische Universität München, Weihenstephaner Steig 16, 85350 Freising, Germany.
authors.forename: Kai
authors.initials: K
authors.lastname: Linke
authors.forename: Nagarajan
authors.initials: N
authors.lastname: Periasamy
authors.forename: Matthias
authors.initials: M
authors.lastname: Ehrmann
authors.forename: Roland
authors.initials: R
authors.lastname: Winter
authors.forename: Rudi F
authors.initials: RF
authors.lastname: Vogel
mesh_terms: D019677:Artificial Gene Fusion; D001426:Bacterial Proteins / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D017930:Genes, Reporter; D006874:Hydrostatic Pressure; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D014157:Transcription Factors; C066719:toxR protein, bacteria; D001616:beta-Galactosidase